ID A0A2G9GHG7_9LAMI Unreviewed; 1070 AA.
AC A0A2G9GHG7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN ORFNames=CDL12_22734 {ECO:0000313|EMBL:PIN04726.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN04726.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIN04726.1}.
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DR EMBL; NKXS01005028; PIN04726.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9GHG7; -.
DR STRING; 429701.A0A2G9GHG7; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279}.
FT DOMAIN 108..750
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 795..958
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1029..1055
FT /note="Zinc finger FPG/IleRS-type"
FT /evidence="ECO:0000259|Pfam:PF06827"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1070 AA; 120466 MW; D7CB79F3B62F608B CRC64;
MAMQNSPYRV LSLRNCSSFR STTAVSLLHL RRSSSARVLS LLHATCYSTC SGIEYGSSSK
RRSQGPVMAA KGKSEGEKQE DGRYKHTIDL PKTAFGLRAN SVVREPEIQK LWDKNQVFKR
VASRNTRGSF VLHDGPPYAN GDLHMGHALN KILKDIINRY KLLQNFQVHY VPGWDCHGLP
IELKVLQSLD QDARKELTPI KLRAKAAKFA KATVKSQMAA FKRYGVWGDW DYPYLTLDPE
YEAAQIEVFG QMALQGYIYR GRKPVHWSPS SRTALAEAEL EYPEGHVSKS MYAIFRLVST
STSCKLLGDF IPNLGLAIWT TTPWTIPSNA AVAVNSKLQY AIIDVQSTSV DTTASSVSKE
KRIGNVLKEH DKLYLVVALD LVPTLEAKWG MKLFVKTTLT GAELENCRYV HPIENRECPV
VVGGDYITTE SGTGLVHTAP GHGQEDYVTG LKYDLPILSP VDDEGIFTEE AGQFSGLSVL
GDGNVAVIEC LDRNLSMIMV EPYKHKYPYD WRTKKPTIFR ATEQWFASVE GFRKAAMDSI
NQVTWIPPQA ENRISSMTSS RSDWCISRQR SWGVPIPVFY HVETKEPLMN EETIDHIKSI
ISQKGSDAWW YMKVEELLPE KYRNEASNYV KGTDTMDVWF DSGSSWAAVL GKRNGLSYPA
DLYLEGTDQH RGWFQSSLLT SIATNGKAPY RGVITHGFVL DEKGFKMSKS LGNVVDPRTV
IEGGKDQKDS FGADVLRLWV SSVDYTGDVM IGPKILRQMS DIYRKLRGTL RFLLGNLHDW
KADYAVPYSD LPMIDQYALF QLESVVKNIK ESYDNYQFFK IFQIIQRFVV VDLSNFYLDV
AKDRLYVGGT TSSTRRSCQT VLATHLLSVV RVIAPILPHL AEDVWQNLPF PFTSEDGNKA
NFVFESKWPV LNKRHLAFPD EEVNFWGTIL ELRTEVNKVL EVARTNKLIG SSLEAKVYLH
ASDDTLVSRL INMCSSDNDA DTLHRIFLTS QVEILPSLEN VTEDKIPCTG EYLIQNTNKV
WIGVSRANGL KCERCWNFSL QVGSYDDHPT LCSRCHSVVS QPTPALAAAS
//
